sam-based wireless sensor node Search Results


pacemaker-based sleep apnea monitoring (sam) algorithm  (MicroPort Scientific Corporation)
90
MicroPort Scientific Corporation pacemaker-based sleep apnea monitoring (sam) algorithm
Pacemaker Based Sleep Apnea Monitoring (Sam) Algorithm, supplied by MicroPort Scientific Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/pacemaker-based sleep apnea monitoring (sam) algorithm/product/MicroPort Scientific Corporation
Average 90 stars, based on 1 article reviews
pacemaker-based sleep apnea monitoring (sam) algorithm - by Bioz Stars, 2026-06
90/100 stars
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sam methyltransferase assay samfluorotm  (G Biosciences)
90
G Biosciences sam methyltransferase assay samfluorotm
Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative <t>methyltransferase</t> activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005
Sam Methyltransferase Assay Samfluorotm, supplied by G Biosciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/sam methyltransferase assay samfluorotm/product/G Biosciences
Average 90 stars, based on 1 article reviews
sam methyltransferase assay samfluorotm - by Bioz Stars, 2026-06
90/100 stars
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picard sam manipulation library  (SourceForge net)
90
SourceForge net picard sam manipulation library
Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative <t>methyltransferase</t> activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005
Picard Sam Manipulation Library, supplied by SourceForge net, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/picard sam manipulation library/product/SourceForge net
Average 90 stars, based on 1 article reviews
picard sam manipulation library - by Bioz Stars, 2026-06
90/100 stars
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sam 4.1  (VBM Medizintechnik)
90
VBM Medizintechnik sam 4.1
Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative <t>methyltransferase</t> activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005
Sam 4.1, supplied by VBM Medizintechnik, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/sam 4.1/product/VBM Medizintechnik
Average 90 stars, based on 1 article reviews
sam 4.1 - by Bioz Stars, 2026-06
90/100 stars
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sam/bigdye xterminatortm bead working solution  (IKA Werke GmbH Co KG)
90
IKA Werke GmbH Co KG sam/bigdye xterminatortm bead working solution
Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative <t>methyltransferase</t> activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005
Sam/Bigdye Xterminatortm Bead Working Solution, supplied by IKA Werke GmbH Co KG, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/sam/bigdye xterminatortm bead working solution/product/IKA Werke GmbH Co KG
Average 90 stars, based on 1 article reviews
sam/bigdye xterminatortm bead working solution - by Bioz Stars, 2026-06
90/100 stars
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sam methyltransferase assay samfluoro™  (G Biosciences)
90
G Biosciences sam methyltransferase assay samfluoro™
Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative <t>methyltransferase</t> activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005
Sam Methyltransferase Assay Samfluoro™, supplied by G Biosciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/sam methyltransferase assay samfluoro™/product/G Biosciences
Average 90 stars, based on 1 article reviews
sam methyltransferase assay samfluoro™ - by Bioz Stars, 2026-06
90/100 stars
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samtools  (SourceForge net)
90
SourceForge net samtools
Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative <t>methyltransferase</t> activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005
Samtools, supplied by SourceForge net, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/samtools/product/SourceForge net
Average 90 stars, based on 1 article reviews
samtools - by Bioz Stars, 2026-06
90/100 stars
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purina 5001 rodent chow  (Purina Mills)
90
Purina Mills purina 5001 rodent chow
Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative <t>methyltransferase</t> activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005
Purina 5001 Rodent Chow, supplied by Purina Mills, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/purina 5001 rodent chow/product/Purina Mills
Average 90 stars, based on 1 article reviews
purina 5001 rodent chow - by Bioz Stars, 2026-06
90/100 stars
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endoscopy-related ml/dl-based samd  (CYBERNET SYSTEMS CO LTD)
90
CYBERNET SYSTEMS CO LTD endoscopy-related ml/dl-based samd
Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative <t>methyltransferase</t> activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005
Endoscopy Related Ml/Dl Based Samd, supplied by CYBERNET SYSTEMS CO LTD, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/endoscopy-related ml/dl-based samd/product/CYBERNET SYSTEMS CO LTD
Average 90 stars, based on 1 article reviews
endoscopy-related ml/dl-based samd - by Bioz Stars, 2026-06
90/100 stars
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pb-based distance-dependent dielectric function  (AUTODOCK GmbH)
90
AUTODOCK GmbH pb-based distance-dependent dielectric function
Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative <t>methyltransferase</t> activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005
Pb Based Distance Dependent Dielectric Function, supplied by AUTODOCK GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/pb-based distance-dependent dielectric function/product/AUTODOCK GmbH
Average 90 stars, based on 1 article reviews
pb-based distance-dependent dielectric function - by Bioz Stars, 2026-06
90/100 stars
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peg based adhesives  (Genzyme)
86
Genzyme peg based adhesives
Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative <t>methyltransferase</t> activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005
Peg Based Adhesives, supplied by Genzyme, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/peg based adhesives/product/Genzyme
Average 86 stars, based on 1 article reviews
peg based adhesives - by Bioz Stars, 2026-06
86/100 stars
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micropatterned dishes biosurfine-awp  (Toyo Gosei Co Ltd)
90
Toyo Gosei Co Ltd micropatterned dishes biosurfine-awp
Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative <t>methyltransferase</t> activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005
Micropatterned Dishes Biosurfine Awp, supplied by Toyo Gosei Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/micropatterned dishes biosurfine-awp/product/Toyo Gosei Co Ltd
Average 90 stars, based on 1 article reviews
micropatterned dishes biosurfine-awp - by Bioz Stars, 2026-06
90/100 stars
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Image Search Results


Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative methyltransferase activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005

Journal: medRxiv

Article Title: EHMT2 LOSS-OF-FUNCTION ALTERATIONS CAUSE A KLEEFSTRA-LIKE SYNDROME

doi: 10.1101/2024.01.10.24300997

Figure Lengend Snippet: Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative methyltransferase activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005

Article Snippet: Histone methyltransferase assays were performed using the fluorescence-based assay SAM Methyltransferase Assay SAMfluoroTM from G-Biosciences that detects the formation of resorufin over time as a result of the methyltransferase reaction.

Techniques: Activity Assay, Mutagenesis, Recombinant, Standard Deviation, Staining, Binding Assay

Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative methyltransferase activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005

Journal: medRxiv

Article Title: EHMT2 LOSS-OF-FUNCTION ALTERATIONS CAUSE A KLEEFSTRA-LIKE SYNDROME

doi: 10.1101/2024.01.10.24300997

Figure Lengend Snippet: Molecular alterations in EHMT2 catalytic domain caused by the p.Ala1077Ser change. A. Measure of cumulative methyltransferase activity over time (seconds) using 250 ng of the catalytic domain of EHMT2 wild type (WT) or p.Ala1077Ser mutant and 2.5 µg of recombinant histone H3 as a substrate. Graph shows the mean and standard deviation of two replicates B. Specific activity in nmol/min/mg of WT and p.Ala1077Ser catalytic domains. Mean and standard deviation of two replicates is shown. C. Coomassie blue stained gel depicting the interaction of WT and Ala1077 catalytic domains with histone H3 peptides amino acids 1 to 21 unmodified (H3), monomethylated at lysine 9 (H3k9me1) and dimethylated at lysine 9 (H3k9me3) D. Quantification of WT and p.Ala1077Ser catalytic domains binding to peptides relative to input. Mean and standard deviation of three quantifications is shown. P-values for comparisons between WT and p.Ala1077Ser correspond to *<0.05, **<0.005 and ***<0.0005

Article Snippet: Histone methyltransferase assays were performed using the fluorescence-based assay SAM Methyltransferase Assay SAMfluoro™ from G-Biosciences that detects the formation of resorufin over time as a result of the methyltransferase reaction.

Techniques: Activity Assay, Mutagenesis, Recombinant, Standard Deviation, Staining, Binding Assay